Corn leaf glutamate synthase : Purification and properties of the enzyme
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概要
- 論文の詳細を見る
An assay for ferredoxin-glutamate synthase is introduced that uses an anion exchange resin to isolate the glutamate formed and subsequent determination with the ninhydrin procedure. The enzyme was purified 200-fold from corn leaves by ammonium sulfate fractionation and chromatography on DEAE-cellulose. DEAE-Sephacel and ferredoxin-Sepharose. The purified enzyme had a specific activity of 14 μmoles glutamate formed min^<-1<mg^<-1< protein. The enzyme has a molecular weight of 160,000. The pH optimum for catalytic activity is 6.9. The isoelectric point is at pH 4.2. The apparent Km values of the enzyme for L-glutamine, 2-oxoglutarate and ferredoxin are 1,100, 240 and 1.7 μM. The enzyme has a high specificity toward these substrates with a stoichiometry between glutamate formation and glutamine consumption. Sulfhydryl reagents, bathophenanthroline, phthalein acids and azaserine produced strong inhibition of the enzyme activity.
- 日本植物生理学会の論文
著者
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Ida Shoji
The Research Institute For Food Science Kyoto University
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Matoh Toru
The Research Institute For Food Science Kyoto University:(present)department Of Agricultural Chemist
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Suzuki Fukuko
The Research Institute for Food Science, Kyoto University
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Suzuki Fukuko
The Research Institute For Food Science Kyoto University
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